1uuv: Difference between revisions

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|PDB= 1uuv |SIZE=350|CAPTION= <scene name='initialview01'>1uuv</scene>, resolution 1.65&Aring;
|PDB= 1uuv |SIZE=350|CAPTION= <scene name='initialview01'>1uuv</scene>, resolution 1.65&Aring;
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IND:INDOLE'>IND</scene> and <scene name='pdbligand=NO:NITROGEN OXIDE'>NO</scene>
|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=IND:INDOLE'>IND</scene>, <scene name='pdbligand=NO:NITROGEN+OXIDE'>NO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Naphthalene_1,2-dioxygenase Naphthalene 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.12.12 1.14.12.12]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Naphthalene_1,2-dioxygenase Naphthalene 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.12.12 1.14.12.12] </span>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uuv OCA], [http://www.ebi.ac.uk/pdbsum/1uuv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uuv RCSB]</span>
}}
}}


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[[Category: Parales, R E.]]
[[Category: Parales, R E.]]
[[Category: Ramaswamy, S.]]
[[Category: Ramaswamy, S.]]
[[Category: EDO]]
[[Category: aromatic hydrocarbons catabolism,]]
[[Category: FE]]
[[Category: FES]]
[[Category: IND]]
[[Category: NO]]
[[Category: SO4]]
[[Category: aromatic hydrocarbons catabolism]]
[[Category: enzyme-substrate complex]]
[[Category: enzyme-substrate complex]]
[[Category: non-heme iron dioxygenase]]
[[Category: non-heme iron dioxygenase]]
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:37:05 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:15:37 2008''

Revision as of 00:15, 31 March 2008

File:1uuv.gif


PDB ID 1uuv

Drag the structure with the mouse to rotate
, resolution 1.65Å
Sites:
Ligands: , , , , ,
Activity: Naphthalene 1,2-dioxygenase, with EC number 1.14.12.12
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



NAPHTHALENE 1,2-DIOXYGENASE WITH NITRIC OXIDE AND INDOLE BOUND IN THE ACTIVE SITE.


OverviewOverview

Nitric oxide (NO) is commonly used as an analogue for dioxygen in structural and spectroscopic studies of oxygen binding and oxygen activation. In this study, crystallographic structures of naphthalene dioxygenase (NDO) in complex with nitric oxide are reported. In the presence of the aromatic substrate indole, NO is bound end-on to the active-site mononuclear iron of NDO. The structural observations correlate well with spectroscopic measurements of NO binding to NDO in solution. However, the end-on binding of NO is in contrast to the recently reported structure of oxygen to the active-site iron of NDO that binds side-on. While NO is a good oxygen analogue with many similarities to O(2), the different binding mode of NO to the active-site iron atom leads to different mechanistic implications. Hence, caution needs to be used in extrapolating NO as an analogue to O(2) binding.

About this StructureAbout this Structure

1UUV is a Protein complex structure of sequences from Pseudomonas putida. Full crystallographic information is available from OCA.

ReferenceReference

NO binding to naphthalene dioxygenase., Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S, J Biol Inorg Chem. 2005 Aug;10(5):483-9. Epub 2005 Sep 23. PMID:15942729

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